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Information on EC 1.8.7.2 - ferredoxin:thioredoxin reductase
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1.8.7.2 ferredoxin:thioredoxin reductaseIUBMB Comments
The enzyme contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-bisphosphatase), EC 3.1.3.37
(sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction.
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Word Map
- 1.8.7.2
- thioredoxins
- chloroplast
- spinach
-
redox-active
- reductases
- epr
- fe-s
-
light-dependent
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one-electron-reduced
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two-electron
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iron-sulfur
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raman
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one-electron
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variable-temperature
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heterodisulfide
- dithiol
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methanosarcina
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ferredoxin-thioredoxin reductase, ferredoxin:thioredoxin reductase, fdx-dependent trx reductase, protein modulase, ferredoxin-dependent thioredoxin reductase, fd-thioredoxin reductase, fdx flavin-thioredoxin reductase, ferredoxin disulfide reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Fdx flavin-thioredoxin reductase
Fdx-dependent thioredoxin reductase
ferredoxin-dependent thioredoxin reductase
FTR
FTRc
iron-sulfur ferredoxin-dependent thioredoxin reductase
Ma_1659
protein modulase
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a complex protein composed of ferredoxin/thioredoxin reductase, ferredoxin, and thioredoxin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+
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2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+
reaction mechanism, overview
2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+
reaction mechanism, overview
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:thioredoxin disulfide oxidoreductase
The enzyme contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-bisphosphatase), EC 3.1.3.37
(sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction.
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CAS REGISTRY NUMBER
COMMENTARY
65589-57-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxidized ferredoxin + thioredoxin f + H+
reduced ferredoxin + thioredoxin f disulfide
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-
-
?
oxidized ferredoxin + thioredoxin m + H+
reduced ferredoxin + thioredoxin m disulfide
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-
-
?
oxidized ferredoxin + thioredoxin z + H+
reduced ferredoxin + thioredoxin z disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-f1 + H+
reduced ferredoxin + thioredoxin-f1 disulfide
-
-
-
-
?
oxidized ferredoxin + thioredoxin-f2 + H+
reduced ferredoxin + thioredoxin-f2 disulfide
-
-
-
-
?
oxidized ferredoxin + thioredoxin-m1 + H+
reduced ferredoxin + thioredoxin-m1 disulfide
-
-
-
-
?
oxidized ferredoxin + thioredoxin-m2 + H+
reduced ferredoxin + thioredoxin-m2 disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-m3 + H+
reduced ferredoxin + thioredoxin-m3 disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-m4 + H+
reduced ferredoxin + thioredoxin-m4 disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-x + H+
reduced ferredoxin + thioredoxin-x disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-y1 + H+
reduced ferredoxin + thioredoxin-y1 disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-y2 + H+
reduced ferredoxin + thioredoxin-y2 disulfide
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-
-
-
?
oxidized ferredoxin + thioredoxin-z + H+
reduced ferredoxin + thioredoxin-z disulfide
-
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
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-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
reduced ferredoxin + thioredoxin disulfide
-
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
oxidized ferredoxin + thioredoxin + H+
-
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
oxidized ferredoxin + thioredoxin + H+
-
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
oxidized ferredoxin + thioredoxin + H+
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-
-
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r
additional information
?
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10 thioredoxin (Trx) isoforms in Arabidopsis thaliana can be clustered into three classes based on the kinetics of the ferredoxin-thioredoxin reductase (FTR)-dependent reduction (high-, middle-, and low-efficiency classes). Analysis of interaction between FTR and Trxs in the complex, structure analyses, detailed overview
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additional information
?
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10 thioredoxin (Trx) isoforms in Arabidopsis thaliana can be clustered into three classes based on the kinetics of the ferredoxin-thioredoxin reductase (FTR)-dependent reduction (high-, middle-, and low-efficiency classes). Analysis of interaction between FTR and Trxs in the complex, structure analyses, detailed overview
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additional information
?
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typical chloroplast thioredoxins (TRXs) include those of types m (four isoforms), f (two isoforms), y (two isoforms), x, and z. The redox regulation of enzymes of the Calvin-Benson cycle (CBC) and show the relevance of f-type TRXs in the light-dependent regulation of carbon fixation
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additional information
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when combined with spinach thylakoid membranes, the components of the ferredoxin-thioredoxin system function in the light activation of the standard target enzymes from chloroplasts, corn NADP-malate dehydrogenase, and spinach fructose 1,6-bisphosphatase, as well as the chloroplast-type fructose 1,6-bisphosphatase from Chlamydomonas. Activity is greatest if ferredoxin and other components of the ferredoxin-thioredoxin system are from Chlamydomonas
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?
additional information
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reduced ferredoxin (Fdx) is the electron donor for the DTR enzyme from cyanobacterium Gloeobacter violaceus (GvDTR)
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additional information
?
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reduced ferredoxin (Fdx) is the electron donor for the DTR enzyme from cyanobacterium Gloeobacter violaceus (GvDTR)
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additional information
?
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reduced ferredoxin (Fdx) is the electron donor for the DTR enzyme from cyanobacterium Gloeobacter violaceus (GvDTR)
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additional information
?
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FTR accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive disulfide to an active thiol form
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?
additional information
?
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midpoint potential of the active site disulfide/dithiol couple is -230 mV
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?
additional information
?
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the catalytic mechanism involves S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxidized ferredoxin + thioredoxin z + H+
reduced ferredoxin + thioredoxin z disulfide
-
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
2 reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
reduced ferredoxin + thioredoxin disulfide
-
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
oxidized ferredoxin + thioredoxin + H+
-
-
-
-
?
reduced ferredoxin + thioredoxin disulfide
oxidized ferredoxin + thioredoxin + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
in each monomer, two conserved Rossmann-type modules form the FAD-binding. The pi-stacking interaction between the side chain of the conserved tryptophan at the C-terminal tail of a monomer and the isoalloxazine ring of the FAD of an adjacent monomer at its re-face. This interaction seems to protect the flavin from the solvent, a distinctive feature of the GvDTR enzyme not found in other flavin thioredoxin reductases. The C-terminal extension stabilizes the semiquinone state of the flavin
4Fe-4S-center
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midpoint potential value of + 340 mV. The midpoint potential value shifts slightly, to + 380 mV, in the N-ethylmaleimide-treated enzyme
4Fe-4S-center
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presence of a unique iron site in the [4Fe-4S] cluster. Site-specific cluster chemistry, involving the formation of a five-coordinate Fe site with two cysteinate ligands, occurs during catalytic cycling of FTR
4Fe-4S-center
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presence of a [Fe4S4]3+ cluster that is coordinated by five cysteinates with little unpaired spin density delocalized onto the cluster-associated cysteine of the active-site disulfide. While the ligation site of the fifth cysteine remains undefined, the best candidate is a cluster bridging sulfide
4Fe-4S-center
-
presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide
4Fe-4S-center
residues Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster
Ferredoxin
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ferredoxin-thioredoxin reductase forms an electrostatically stabilized 1:1 complex with ferredoxin. Chemical modification of three or four carboxyl groups on ferredoxin has little effect on its interaction with ferredoxin-thioredoxin reductase. The ferredoxin domain that binds ferredoxin-thioredoxin reductase is not completely identical to that involved in binding other ferredoxin-dependent enzymes
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Ferredoxin
Fdx, iron-sulfur ferredoxin, enzyme-Fdx interaction analysis, overview. Investigation of GvDTR and GvFdx1 or GvFdx2 as functional redox partners by analyzing the reduction of photosynthetic m-type thioredoxin (Trxm) in a mixture containing NADPH, the redox pair Anabaena ferredoxin-NADP+ reductase (AnFNR)/GvFdx1 or AnFNR/GvFdx2, GvDTR, and Gloeobacter Trx-m (GvTrxm). The redox state of GvTrx-m is examined with the thiol-specific reagent 4-acetamido-40-maleimidyldistilbene-2,2'-disulfonic acid (AMS), separating the reduced and oxidized proteins with nonreducing SDS-PAG.Only GvFdx1 with the complete reactants significantly increases the reduced/oxidized ratio of GvTrx-m, prompting the conclusion that GvFFTR interacts with GvFdx1 but not with GvFdx2, which has a unique C-terminal extension. GvFdx1 is a functional electron-delivering partner for GvDTR. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. GvFdx1 (petF, gvip492) and GvFdx2 (gvip440) are recombinantly expressed as N-terminally His8-tagged proteins, with a TEV cleavage site preceding the Fdx sequence, in Escherichia coli Rosetta (DE3) pLys cells
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
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presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide
Fe2+
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nature, properties, and function of the Fe-S cluster in spinach FTR, overview. [4Fe-4S]2+ cluster covalently attached through a cluster sulfide to a cysteine-based thiyl radical formed on one of the active-site thiols, and at least partial cluster oxidation to the [4Fe-4S]3+ state. Proposed canonical structures for the Fe-S cluster in N-ethylmaleimide-modified spinach FTR, overview. Detailed spectroscopic analysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
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spinach ferredoxin:thioredoxin reductase reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin exhibits a slowly relaxing S = 1/2 resonance identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide. N-ethylmaleimide-TR is a stable analogue of a one-electron-reduced enzymatic intermediate
N-ethylmaleimide
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the midpoint potential value of the high-potential redox center shifts from 340 mV to + 380 mV, in the N-ethylmaleimide-treated enzyme. Treatment of the enzyme with N-ethylmaleimide eliminates the component with the - 230 mV midpoint potential
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
reduced ferredoxin
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ferredoxin modified by treatment with glycine ethyl ester in the presence of 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, pH 7.9
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chimeric protein containing a plant-type ferredoxin/thioredoxin reductase-like catalytic domain in the N-terminal region and a bacterial-like rubredoxin domain in the C-terminal region
UniProt
brenda
chimeric protein containing a plant-type ferredoxin/thioredoxin reductase-like catalytic domain in the N-terminal region and a bacterial-like rubredoxin domain in the C-terminal region
UniProt
brenda
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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transcripts of the catalytic subunit FTR-c are detected in all tissues examined, including roots, leaves, flowers, fruits, and seeds
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
some cyanobacteria, such as the thylakoid-less Gloeobacter and the ocean-dwelling green oxyphotobacterium Prochlorococcus, lack thioredoxin reductase flavoenzyme (NTR) and (Fdx)-dependent thioredoxin reductase (FTR) but contain a thioredoxin reductase flavoenzyme (formerly tentatively called deeply-rooted thioredoxin reductase or DTR), whose electron donor is Fdx. This cyanobacterial enzyme belongs to the Fdx flavin-thioredoxin reductase (FFTR) family, originally described in the anaerobic bacterium Clostridium pasteurianum. Accordingly, the enzyme hitherto termed DTR is renamed FFTR. The FFTR is spread within the cyanobacteria phylum. By substituting for FTR, it connects the reduction of target proteins to photosynthesis. FFTR acquisition constitutes a mechanism of evolutionary adaptation in marine phytoplankton such as Prochlorococcus that live in low-iron environments. Cyanobacterial Fdx-dependent thioredoxin reductases might have diverged early in the evolution into flavo- or metalloenzymes
evolution
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some cyanobacteria, such as the thylakoid-less Gloeobacter and the ocean-dwelling green oxyphotobacterium Prochlorococcus, lack thioredoxin reductase flavoenzyme (NTR) and (Fdx)-dependent thioredoxin reductase (FTR) but contain a thioredoxin reductase flavoenzyme (formerly tentatively called deeply-rooted thioredoxin reductase or DTR), whose electron donor is Fdx. This cyanobacterial enzyme belongs to the Fdx flavin-thioredoxin reductase (FFTR) family, originally described in the anaerobic bacterium Clostridium pasteurianum. Accordingly, the enzyme hitherto termed DTR is renamed FFTR. The FFTR is spread within the cyanobacteria phylum. By substituting for FTR, it connects the reduction of target proteins to photosynthesis. FFTR acquisition constitutes a mechanism of evolutionary adaptation in marine phytoplankton such as Prochlorococcus that live in low-iron environments. Cyanobacterial Fdx-dependent thioredoxin reductases might have diverged early in the evolution into flavo- or metalloenzymes
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malfunction
Arabidopsis thaliana mutants with decreased contents of the catalytic subunit of FTR (FTRc), hence with impaired fuel of electrons into the pathway, show severe chlorosis in leaf sectors near the petiole, similar to the phenotype of mutant plants with lower FTR activity. In contrast, the deficiency of individual TRXs has low effect on growth phenotype indicating functional redundancy of the different plastid TRXs, except TRX z since mutants lacking this TRX show an albino phenotype
malfunction
deletion of the C-terminal tail does not significantly affect structure and both GvDTR and GvDTR_DELTAtail proteins are properly folded. The mutant enzyme is able to reduce Trx when a non-physiological electron donor (dithionite) is used
malfunction
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deletion of the C-terminal tail does not significantly affect structure and both GvDTR and GvDTR_DELTAtail proteins are properly folded. The mutant enzyme is able to reduce Trx when a non-physiological electron donor (dithionite) is used
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metabolism
the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. In addition, chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. NTRC is required for the activity of TRXs. Genetic approaches using mutants of Arabidopsis thaliana in combination with biochemical and physiological studies show that both redox systems, NTRC and FDX-FTR-TRXs, participate in fine-tuning chloroplast performance in response to changes in light intensity. Moreover, these studies reveal the participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control of the reducing activity of chloroplast TRXs as well as in the rapid oxidation of stromal enzymes upon darkness. Analysis of functional relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems for fine-tuning chloroplast performance in response to changes in light intensity and darkness, overview. NTRC and FDX-FTR-TRXs pathway are integrated by the redox balance of 2-Cys PRXs. Redox regulation is an additional layer of control of the signaling function of the chloroplast
metabolism
thiol-based redox regulation is a mechanism for controlling metabolic pathways in chloroplasts. Thioredoxin (Trx) possesses a pair of redox-active cysteines that activates specific enzymes in a light-dependent manner. The redox level of Trx is maintained by ferredoxin-Trx reductase (FTR) and ferredoxin (Fd), the latter being the final electron acceptor in the photosynthetic electron transport chain. In this Fd/Trx cascade, electrons are sequentially transmitted from photosystem I, via Fd, FTR, and Trx, to target enzymes such as fructose-1,6-bisphosphatase, sedoheptulose-bisphosphatase, NADP-malate dehydrogenase, or 2-Cys peroxiredoxins
physiological function
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ferredoxin-thioredoxin reductase is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive disulfide to an active thiol form
physiological function
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identification of ferredoxin-thioredoxin reductase and NADPH-thioredoxin reductase, and four typical thioredoxin isoforms identified by genomic analysis. The NADPH-thioredoxin reductase pathway is important for the antioxidant system, whereas the ferredoxin-thioredoxin reductase pathway may play a more important role in the control of cell growth rate. The gene product of slr0623, the homolog of m-type thioredoxin in higher plants, is the most abundant thioredoxin, and accumulation of thioredoxin isoforms occurs dependent on the expression of the other redox-related proteins
physiological function
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study on mutant lines in which one of two genes encoding FTRA variable subunit is disrupted by T-DNA insertion. In FTRA1mutants, the absence of the corresponding transcript is not compensated by the increase in the level of FTRA2 mRNA. Mutant plants exhibit phenotypic perturbations when compared with wild-type plants. Disruptants are significantly more sensitive to oxidative stress as imposed under high light or in the presence of paraquat. In the leaves of mutants placed under normal culture conditions, NADP-dependent malate dehydrogenase activation rate is abnormally low. A partially compensating increase of the enzyme activity is found as well as a higher amount of 2-cysperoxiredoxin
physiological function
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virus-induced gene silencing of the catalytic subunit FTR-c results in necrotic lesions with typical cell death symptoms and reactive oxygen species production in tomato leaves. These FTR-c-silenced plants display enhanced disease resistance against bacterial pathogens, specifically Pseudomonas syringae pv. tomato DC3000, by the induction of defense-related genes such as PR-1, PR-2, PR-5, GlucA, Chi3, and Chi9
physiological function
ferredoxin:thioredoxin reductase is the key enzyme of the ferredoxid-thioredoxin system, and is involved in the light regulation of carbon metabolism in oxygenic photosynthesis catalyzing the reduction of thioredoxins with light-generated electrons
physiological function
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the enzyme is required for proper chloroplast development and is involved in the regulation of plastid gene expression. The enzyme and thopredoxin z act together in the regulation of plastid-encoded RNA polymerase function during early stages of chloroplast development
physiological function
photosynthetic electron transport occurs on the thylakoid membrane of chloroplasts. Ferredoxin (Fd), the final acceptor in the electron transport chain, distributes electrons to several Fd-dependent enzymes including Fd-thioredoxin reductase (FTR). A cascade from Fd to FTR further reduces thioredoxin (Trx), which tunes the activity of target metabolic enzymes eventually in a light-dependent manner
physiological function
regulation of enzyme activity based on thiol-disulfide exchange is a regulatory mechanism in which the protein disulfide reductase activity of thioredoxins (TRXs) plays a central role. Plant chloroplasts are equipped with a complex set of up to 20 TRXs and TRX-like proteins, the activity of which is supported by reducing power provided by photosynthetically reduced ferredoxin (FDX) with the participation of a FDX-dependent TRX reductase (FTR). The complex redox network composed of the FDX-FTR-TRXs pathway links redox regulation to light. Therefore, the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. Involvement of redox regulation in chloroplast retrograde signaling modulates early stages of plant development and response to environmental stress, overview. Ferredoxin, FDX, the final acceptor of the photosynthetic electron transport chain, fuels reducing equivalents to plastid thioredoxins (TRXs) with the participation of FTR
physiological function
thioredoxin reductases control the redox state of thioredoxins (Trxs), ubiquitous proteins that regulate a spectrum of enzymes by dithiol-disulfide exchange reactions. In most organisms, Trx is reduced by NADPH via a thioredoxin reductase flavoenzyme (NTR), but in oxygenic photosynthetic organisms, this function can also be performed by an iron-sulfur ferredoxin (Fdx)-dependent thioredoxin reductase (FTR) that links light to metabolic regulation. The FFTR/Trx system of Gloeobacter is able to reduce CP12, a small protein functional in the regulation of two enzymes of the Calvin-Benson cycle in oxygenic photosynthetic organisms-phosphoribulokinase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). FFTR can substitute for FTR in light-linked redox regulation in Gloeobacter
physiological function
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thioredoxin reductases control the redox state of thioredoxins (Trxs), ubiquitous proteins that regulate a spectrum of enzymes by dithiol-disulfide exchange reactions. In most organisms, Trx is reduced by NADPH via a thioredoxin reductase flavoenzyme (NTR), but in oxygenic photosynthetic organisms, this function can also be performed by an iron-sulfur ferredoxin (Fdx)-dependent thioredoxin reductase (FTR) that links light to metabolic regulation. The FFTR/Trx system of Gloeobacter is able to reduce CP12, a small protein functional in the regulation of two enzymes of the Calvin-Benson cycle in oxygenic photosynthetic organisms-phosphoribulokinase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). FFTR can substitute for FTR in light-linked redox regulation in Gloeobacter
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additional information
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role for Fe-S clusters in the enzyme mechanism involving both the stabilization of a thiyl radical intermediate and cluster site-specific chemistry involving a bridging sulfide
additional information
crystallographic structure of the transient complex between the plant-type Fdx1 and the thioredoxin reductase flavoenzyme from Gloeobacter violaceus. A unique feature of GvDTR is the presence of a C-terminal tail with a conserved aromatic amino acid that stacks onto the isoalloxazine ring of the FAD of the adjacent monomer. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. Conformations adopted by GvDTR during its catalytic cycle, detailed overview
additional information
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crystallographic structure of the transient complex between the plant-type Fdx1 and the thioredoxin reductase flavoenzyme from Gloeobacter violaceus. A unique feature of GvDTR is the presence of a C-terminal tail with a conserved aromatic amino acid that stacks onto the isoalloxazine ring of the FAD of the adjacent monomer. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. Conformations adopted by GvDTR during its catalytic cycle, detailed overview
additional information
superposition of the FTR structure with/without Trx showed no main chain structural changes upon complex formation. There is no significant conformational change for single and complexed Trx-m structures. Nonetheless, the interface of FTR:Trx complexes displayed significant variation. Comparative analysis of the three structures shows two types of intermolecular interactions: (i) common interactions shared by all three complexes and (ii) isoform-specific interactions, which might be important for fine-tuning FTR:Trx activity
additional information
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superposition of the FTR structure with/without Trx showed no main chain structural changes upon complex formation. There is no significant conformational change for single and complexed Trx-m structures. Nonetheless, the interface of FTR:Trx complexes displayed significant variation. Comparative analysis of the three structures shows two types of intermolecular interactions: (i) common interactions shared by all three complexes and (ii) isoform-specific interactions, which might be important for fine-tuning FTR:Trx activity
additional information
-
crystallographic structure of the transient complex between the plant-type Fdx1 and the thioredoxin reductase flavoenzyme from Gloeobacter violaceus. A unique feature of GvDTR is the presence of a C-terminal tail with a conserved aromatic amino acid that stacks onto the isoalloxazine ring of the FAD of the adjacent monomer. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. Conformations adopted by GvDTR during its catalytic cycle, detailed overview
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Show AA Sequence and Transmembrane Helices (3764 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10939
-
x * ? + x * 10939, variable subunit, without known catalytic function, calculated
12669
-
x * ? + x * 12669, subunit A, without a known catalytic function, calculated
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
alpha/beta, peptide mapping for localization of labeled cysteinyl residues, overview
heterodimer
homodimer
additional information
?
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x * ? + x * 12669, subunit A, without a known catalytic function, calculated
?
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x * ? + x * 10939, variable subunit, without known catalytic function, calculated
homodimer